Abstract
The immunosuppressant cyclosporin-Δ (CsA) has been crystallized in complex with the bovine form of its major receptor protein cyclophilin (CyP) in three different forms by the hanging-drop vapor diffusion method. A hexagonal crystal form (P6122 or P6522; a = b = 110 Å, c = 440 Å) diffracts to 4 Å resolution. Orthorhombie (P212121 or P21212; a = - 154·3 Å, b = 163·3 Å, c = 94·7 Å), and monoclinic (P21; a = 70·0 Å, b = 162·5 Å, c = 94·7, beta = 100·0°) forms diffract to 2·2 Å resolution. Self-rotation function analysis of the orthorhombic and monoclinic forms shows 52 point group local symmetry for both. A previously reported tetragonal crystal form of the complex also shares this local symmetry, suggesting that the observed motif may pre-exist in solution.
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